ITF2_CANLF
ID ITF2_CANLF Reviewed; 642 AA.
AC P15881;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Transcription factor 4;
DE Short=TCF-4;
DE AltName: Full=Immunoglobulin transcription factor 2;
DE Short=ITF-2;
DE AltName: Full=Thyroglobulin promoter transcription factor TFE;
GN Name=TCF4; Synonyms=ITF2, TFE;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=1840650; DOI=10.1093/nar/19.5.1121;
RA Damagnez V., de Recondo A.-M., Baldacci G.;
RT "Cloning and sequence analysis of TFE, a helix-loop-helix transcription
RT factor able to recognize the thyroglobulin gene promoter in vitro.";
RL Nucleic Acids Res. 19:1121-1127(1991).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE.
RX PubMed=2320428; DOI=10.1093/nar/18.5.1301;
RA Javaux F., Vassart G., Christophe D.;
RT "Nucleotide sequence of a putative transcription factor recognizing the
RT thyroglobulin promoter.";
RL Nucleic Acids Res. 18:1301-1301(1990).
CC -!- FUNCTION: Transcription factor that binds to the immunoglobulin
CC enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal
CC differentiation. Activates transcription by binding to the E box (5'-
CC CANNTG-3') (By similarity). Binds to the thyroglobulin promoter.
CC {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Forms homo- or heterooligomers with myogenin. Interacts with
CC HIVEP2. Interacts with NEUROD2 (By similarity). Interacts with AGBL1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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DR EMBL; X51448; CAA35812.1; -; mRNA.
DR PIR; S34416; S34416.
DR RefSeq; NP_001003268.1; NM_001003268.1.
DR AlphaFoldDB; P15881; -.
DR STRING; 9612.ENSCAFP00000000209; -.
DR PaxDb; P15881; -.
DR GeneID; 403949; -.
DR KEGG; cfa:403949; -.
DR CTD; 6925; -.
DR eggNOG; KOG3910; Eukaryota.
DR InParanoid; P15881; -.
DR OrthoDB; 571132at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..642
FT /note="Transcription factor 4"
FT /id="PRO_0000127255"
FT DOMAIN 539..592
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..59
FT /note="Essential for MYOD1 inhibition"
FT /evidence="ECO:0000250"
FT REGION 311..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..375
FT /note="Leucine-zipper"
FT REGION 444..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..617
FT /note="Class A specific domain"
FT REGION 609..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15884"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15884"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15884"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62655"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15884"
SQ SEQUENCE 642 AA; 68355 MW; F9B4F7061059A733 CRC64;
MFSPPVSSGK NGPTSLASGH FTGSNVEDRS SSGSWGNGGH PSPSRNYGDG TPYDHMTSRD
LGSHDNLSPP FVNSRIQSKT ERGSYSSYGR ESNLQGCHQS LLGGDMDMGT PGTLSPTKPG
SQYYQYSSNN PRRRPLHSSA MEVQTKKVRK VPPGLPSSVY APSASTADYN RDSPGYPSSK
PAASTFPSSF FMQDGHHSSD PWSSSSGMNQ PGYGGMLGSS SHIPQSSSYC SLHPHERLSY
PSHSSADINS SLPPMSTFHR SGTNHYSTSS CTPPANGTDS IMANRGSGAA GSSQTGDALG
KALASIYSPD HTNNSFSSNP STPVGSPPSL SAGTAVWSRN GGQASSSPNY EGPLHSLQSR
IEDRLERLDD AIHVLRNHAV GPSTAMPGGH GDMHGIIGPS HNGAMGGLGS GYGTGLLSAN
RHSLMVGAHR EDGVALRGSH SLVPNQVPVP QLPVQSATSP DLNPPQDPYR GMPPGLQGQS
VSSGSSEIKS DDEGDENLQD TKSSEDKKLD DDKKDIKSIT SNNDDEDLTP EQKAEREKER
RMANNARERL RVRDINEAFK ELGRMVQLHL KSDKPQTKLL ILHQAVAVIL SLEQQVRERN
LNPKAACLKR REEEKVSSEP PPLSLAGPHP GMGDASNHMG QM
